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Actinohivin, a novel anti-HIV protein from an actinomycete that inhibits syncytium formation: isolation, characterization, and biological activities.
Chiba, H; Inokoshi, J; Okamoto, M; Asanuma, S; Iwama, M; Mizumoto, K; Tanaka, H; Oheda, M; Fujita, K; Nakashima, H; Shinose, M; Takahashi, Y; Omura, S.
Afiliación
  • Chiba H; School of Pharmaceutical Sciences, Kitasato University, 5-9-1 Shirokane, Minato-ku, Tokyo, 108-8641, Japan.
Biochem Biophys Res Commun ; 282(2): 595-601, 2001 Mar 30.
Article en En | MEDLINE | ID: mdl-11401502
Blocking human immunodeficiency virus (HIV) entry into target cells is an important goal of HIV and acquired immune deficiency syndrome (AIDS) therapies. We have searched for anti-HIV substances from microorganisms using a syncytium formation assay system constructed with HeLa/CD4/Lac-Z and HeLa/T-env/Tat cells. We discovered a novel anti-HIV protein that inhibits syncytium formation, designated as actinohivin, from a cultured broth of a soil isolate, actinomycete strain K97-0003. ESI mass spectrometry of actinohivin isolated from the culture filtrate showed an ion with molecular mass of 12,520.3 Da. The amino acid sequence was determined by N-terminal Edman degradation of the intact protein and peptide fragments formed by endoproteinase digestions. Actinohivin consists of a 114-amino-acid chain that exhibits internal sequence triplication. Actinohivin inhibited both T-cell and macrophage tropic syncytium formation, with IC(50) values of 60 and 700 nM, respectively, and the cytopathic effect of HIV-1(IIIB) in MT-4 cells, with IC(50) value of 230 nM.
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Actinomycetales / Fármacos Anti-VIH Límite: Humans Idioma: En Revista: Biochem Biophys Res Commun Año: 2001 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Estados Unidos
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Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Actinomycetales / Fármacos Anti-VIH Límite: Humans Idioma: En Revista: Biochem Biophys Res Commun Año: 2001 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Estados Unidos